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Protein

Microsomal triglyceride transfer protein large subunit

Gene

MTTP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transport of triglyceride, cholesteryl ester, and phospholipid between phospholipid surfaces (PubMed:23475612, PubMed:8939939, PubMed:26224785, PubMed:25108285, PubMed:22236406). Required for the secretion of plasma lipoproteins that contain apolipoprotein B (PubMed:23475612, PubMed:8939939, PubMed:26224785).5 Publications

GO - Molecular functioni

  • lipid binding Source: UniProtKB-KW
  • lipid transporter activity Source: UniProtKB
  • phospholipid transporter activity Source: UniProtKB
  • protein heterodimerization activity Source: UniProtKB

GO - Biological processi

  • lipid metabolic process Source: ProtInc
  • lipoprotein biosynthetic process Source: Reactome
  • phospholipid transport Source: UniProtKB
  • plasma lipoprotein particle assembly Source: UniProtKB
  • triglyceride transport Source: UniProtKB
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Lipid-binding

Enzyme and pathway databases

ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.

Chemistry

SwissLipidsiSLP:000000411.

Names & Taxonomyi

Protein namesi
Recommended name:
Microsomal triglyceride transfer protein large subunit
Gene namesi
Name:MTTP
Synonyms:MTP
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 4

Organism-specific databases

HGNCiHGNC:7467. MTTP.

Subcellular locationi

GO - Cellular componenti

  • endoplasmic reticulum Source: UniProtKB
  • endoplasmic reticulum lumen Source: Reactome
  • receptor complex Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Endoplasmic reticulum

Pathology & Biotechi

Involvement in diseasei

Abetalipoproteinemia (ABL)7 Publications
The disease is caused by mutations affecting the gene represented in this entry.
Disease descriptionAn autosomal recessive disorder of lipoprotein metabolism. Affected individuals produce virtually no circulating apolipoprotein B-containing lipoproteins (chylomicrons, VLDL, LDL, lipoprotein(A)). Malabsorption of the antioxidant vitamin E occurs, leading to spinocerebellar and retinal degeneration.
See also OMIM:200100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti169 – 1691D → V in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 1 Publication
VAR_074553
Natural varianti264 – 2641G → R in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity. 1 Publication
VAR_074554
Natural varianti435 – 4351L → H in ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity. 1 Publication
VAR_074555
Natural varianti528 – 5281Y → H in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication
VAR_074556
Natural varianti540 – 5401R → C in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication
VAR_074557
Natural varianti540 – 5401R → H in ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 4 Publications
VAR_010642
Natural varianti590 – 5901S → I in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_010643
Natural varianti649 – 6491N → S in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity. 1 Publication
VAR_074558
Natural varianti746 – 7461G → E in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_010644
Natural varianti780 – 7801N → Y in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_014019

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi169 – 1691D → E: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB or P4HB/PDI, does partially reduce phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication
Mutagenesisi187 – 1871K → L: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication
Mutagenesisi187 – 1871K → R: No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion. 1 Publication
Mutagenesisi189 – 1891K → L: No loss on localization to the endoplasmic reticulum and does not reduce interaction with APOB, but inhibits interaction with P4HB/PDI, phospholipid or triglyceride transfer activity and apolipoprotein B secretion. 1 Publication
Mutagenesisi189 – 1891K → R: No loss on localization to the endoplasmic reticulum, does not reduce interaction with APOB or P4HB/PDI, partially inhibits triglyceride transfer activity, does not inhibit phospholipid transfer activity and apolipoprotein B secretion. 1 Publication
Mutagenesisi435 – 4351L → E: No loss on localization to the endoplasmic reticulum. Inhibits triglyceride transfer activity. 1 Publication
Mutagenesisi435 – 4351L → V: No loss on localization to the endoplasmic reticulum. Does not inhibit triglyceride transfer activity. 1 Publication
Mutagenesisi528 – 5281Y → F: Does not inhibit triglyceride transfer activity. 1 Publication
Mutagenesisi528 – 5281Y → K: Inhibits triglyceride transfer activity. 1 Publication
Mutagenesisi540 – 5401R → A: Reduces strongly triglyceride transfer activity. 1 Publication
Mutagenesisi540 – 5401R → K: Does not inhibit triglyceride transfer activity. 1 Publication
Mutagenesisi540 – 5401R → K: Does not inhibit triglyceride transfer activity and apolipoprotein B secretion. 2 Publications
Mutagenesisi878 – 8781C → S: Inhibits triglyceride transfer activity. 1 Publication

Keywords - Diseasei

Disease mutation

Organism-specific databases

MalaCardsiMTTP.
MIMi200100. phenotype.
Orphaneti14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBiPA164742099.

Chemistry

ChEMBLiCHEMBL2364681.
DrugBankiDB01094. Hesperetin.
DB08827. Lomitapide.

Polymorphism and mutation databases

BioMutaiMTTP.
DMDMi1709167.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 1818Sequence analysisAdd
BLAST
Chaini19 – 894876Microsomal triglyceride transfer protein large subunitPRO_0000041593Add
BLAST

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP55157.
PaxDbiP55157.
PRIDEiP55157.

PTM databases

iPTMnetiP55157.
PhosphoSiteiP55157.

Expressioni

Tissue specificityi

Liver and small intestine. Also found in ovary, testis and kidney.1 Publication

Inductioni

Positively regulated by cholesterol and negatively regulated by insulin.1 Publication

Gene expression databases

BgeeiP55157.
CleanExiHS_MTTP.
ExpressionAtlasiP55157. baseline and differential.
GenevisibleiP55157. HS.

Organism-specific databases

HPAiHPA054862.

Interactioni

Subunit structurei

Heterodimer; heterodimerizes with the protein disulfide isomerase (P4HB/PDI) (PubMed:23475612, PubMed:26224785, PubMed:25108285). Interacts with APOB (PubMed:26224785, PubMed:25108285).3 Publications

GO - Molecular functioni

  • protein heterodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi110641. 3 interactions.
MINTiMINT-1537333.
STRINGi9606.ENSP00000265517.

Chemistry

BindingDBiP55157.

Structurei

3D structure databases

ProteinModelPortaliP55157.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini28 – 659632VitellogeninPROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Contains 1 vitellogenin domain.PROSITE-ProRule annotation

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiKOG4337. Eukaryota.
ENOG410YKCW. LUCA.
GeneTreeiENSGT00390000011412.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiP55157.
KOiK14463.
PhylomeDBiP55157.
TreeFamiTF328754.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view]
PfamiPF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P55157-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MILLAVLFLC FISSYSASVK GHTTGLSLNN DRLYKLTYST EVLLDRGKGK
60 70 80 90 100
LQDSVGYRIS SNVDVALLWR NPDGDDDQLI QITMKDVNVE NVNQQRGEKS
110 120 130 140 150
IFKGKSPSKI MGKENLEALQ RPTLLHLIHG KVKEFYSYQN EAVAIENIKR
160 170 180 190 200
GLASLFQTQL SSGTTNEVDI SGNCKVTYQA HQDKVIKIKA LDSCKIARSG
210 220 230 240 250
FTTPNQVLGV SSKATSVTTY KIEDSFVIAV LAEETHNFGL NFLQTIKGKI
260 270 280 290 300
VSKQKLELKT TEAGPRLMSG KQAAAIIKAV DSKYTAIPIV GQVFQSHCKG
310 320 330 340 350
CPSLSELWRS TRKYLQPDNL SKAEAVRNFL AFIQHLRTAK KEEILQILKM
360 370 380 390 400
ENKEVLPQLV DAVTSAQTSD SLEAILDFLD FKSDSSIILQ ERFLYACGFA
410 420 430 440 450
SHPNEELLRA LISKFKGSIG SSDIRETVMI ITGTLVRKLC QNEGCKLKAV
460 470 480 490 500
VEAKKLILGG LEKAEKKEDT RMYLLALKNA LLPEGIPSLL KYAEAGEGPI
510 520 530 540 550
SHLATTALQR YDLPFITDEV KKTLNRIYHQ NRKVHEKTVR TAAAAIILNN
560 570 580 590 600
NPSYMDVKNI LLSIGELPQE MNKYMLAIVQ DILRFEMPAS KIVRRVLKEM
610 620 630 640 650
VAHNYDRFSR SGSSSAYTGY IERSPRSAST YSLDILYSGS GILRRSNLNI
660 670 680 690 700
FQYIGKAGLH GSQVVIEAQG LEALIAATPD EGEENLDSYA GMSAILFDVQ
710 720 730 740 750
LRPVTFFNGY SDLMSKMLSA SGDPISVVKG LILLIDHSQE LQLQSGLKAN
760 770 780 790 800
IEVQGGLAID ISGAMEFSLW YRESKTRVKN RVTVVITTDI TVDSSFVKAG
810 820 830 840 850
LETSTETEAG LEFISTVQFS QYPFLVCMQM DKDEAPFRQF EKKYERLSTG
860 870 880 890
RGYVSQKRKE SVLAGCEFPL HQENSEMCKV VFAPQPDSTS SGWF
Length:894
Mass (Da):99,351
Last modified:October 1, 1996 - v1
Checksum:iB20260C136BDAB9F
GO
Isoform 2 (identifier: P55157-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     134-151: EFYSYQNEAVAIENIKRG → GRLDSTTFSPTSYFSSLQ
     152-894: Missing.

Note: No experimental confirmation available.
Show »
Length:151
Mass (Da):16,865
Checksum:iF0A042FD95FA8F3A
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti585 – 5851F → L in CAA42200 (PubMed:8361539).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti95 – 951Q → H.1 Publication
Corresponds to variant rs61733139 [ dbSNP | Ensembl ].
VAR_014016
Natural varianti98 – 981E → D.
Corresponds to variant rs2306986 [ dbSNP | Ensembl ].
VAR_052961
Natural varianti128 – 1281I → T.2 Publications
Corresponds to variant rs3816873 [ dbSNP | Ensembl ].
VAR_014017
Natural varianti166 – 1661N → S.
Corresponds to variant rs3792683 [ dbSNP | Ensembl ].
VAR_052962
Natural varianti168 – 1681V → I Rare polymorphism. 1 Publication
Corresponds to variant rs61750974 [ dbSNP | Ensembl ].
VAR_022658
Natural varianti169 – 1691D → V in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with APOB; inhibits interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 1 Publication
VAR_074553
Natural varianti244 – 2441Q → E.1 Publication
Corresponds to variant rs17599091 [ dbSNP | Ensembl ].
VAR_014018
Natural varianti264 – 2641G → R in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; does not reduce triglyceride transfer activity. 1 Publication
VAR_074554
Natural varianti297 – 2971H → Q Polymorphism; does not inhibit apolipoprotein B secretion. 3 Publications
Corresponds to variant rs2306985 [ dbSNP | Ensembl ].
VAR_010640
Natural varianti354 – 3541E → Q.
Corresponds to variant rs12933 [ dbSNP | Ensembl ].
VAR_014916
Natural varianti384 – 3841D → A Polymorphism; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; reduces phospholipid or triglyceride transfer activity; does not inhibit apolipoprotein B secretion. 2 Publications
Corresponds to variant rs17029215 [ dbSNP | Ensembl ].
VAR_010641
Natural varianti435 – 4351L → H in ABL; no loss on localization to the endoplasmic reticulum; inhibits triglyceride transfer activity. 1 Publication
VAR_074555
Natural varianti528 – 5281Y → H in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication
VAR_074556
Natural varianti540 – 5401R → C in ABL; does not reduce interaction with P4HB/PDI and APOB; inhibits triglyceride transfer activity. 1 Publication
VAR_074557
Natural varianti540 – 5401R → H in ABL; no loss on localization to the endoplasmic reticulum; reduces interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 4 Publications
VAR_010642
Natural varianti590 – 5901S → I in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_010643
Natural varianti649 – 6491N → S in ABL; unknown pathological significance; does not reduce interaction with P4HB/PDI and APOB; reduces triglyceride transfer activity. 1 Publication
VAR_074558
Natural varianti746 – 7461G → E in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_010644
Natural varianti780 – 7801N → Y in ABL; no loss on localization to the endoplasmic reticulum; does not reduce interaction with P4HB/PDI; inhibits phospholipid or triglyceride transfer activity; inhibits apolipoprotein B secretion. 2 Publications
VAR_014019

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei134 – 15118EFYSY…NIKRG → GRLDSTTFSPTSYFSSLQ in isoform 2. 1 PublicationVSP_056325Add
BLAST
Alternative sequencei152 – 894743Missing in isoform 2. 1 PublicationVSP_056326Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75500 mRNA. Translation: CAA53217.1.
X59657 mRNA. Translation: CAA42200.1.
X83013
, X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
AK290793 mRNA. Translation: BAF83482.1.
AC083902 Genomic DNA. No translation available.
BC062696 mRNA. Translation: AAH62696.1.
BC125110 mRNA. Translation: AAI25111.1.
BC125111 mRNA. Translation: AAI25112.1.
CCDSiCCDS3651.1. [P55157-1]
PIRiI38047.
RefSeqiNP_000244.2. NM_000253.3. [P55157-1]
NP_001287714.1. NM_001300785.1.
UniGeneiHs.195799.

Genome annotation databases

EnsembliENST00000265517; ENSP00000265517; ENSG00000138823. [P55157-1]
ENST00000422897; ENSP00000407350; ENSG00000138823. [P55157-2]
ENST00000457717; ENSP00000400821; ENSG00000138823. [P55157-1]
GeneIDi4547.
KEGGihsa:4547.
UCSCiuc003hvb.4. human. [P55157-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X75500 mRNA. Translation: CAA53217.1.
X59657 mRNA. Translation: CAA42200.1.
X83013
, X83014, X83015, X83016, X83017, X83018, X83019, X83020, X83021, X83022, X83023, X83024, X83025, X83026, X83027, X83028, X83029, X83030 Genomic DNA. Translation: CAA58142.1.
AK290793 mRNA. Translation: BAF83482.1.
AC083902 Genomic DNA. No translation available.
BC062696 mRNA. Translation: AAH62696.1.
BC125110 mRNA. Translation: AAI25111.1.
BC125111 mRNA. Translation: AAI25112.1.
CCDSiCCDS3651.1. [P55157-1]
PIRiI38047.
RefSeqiNP_000244.2. NM_000253.3. [P55157-1]
NP_001287714.1. NM_001300785.1.
UniGeneiHs.195799.

3D structure databases

ProteinModelPortaliP55157.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110641. 3 interactions.
MINTiMINT-1537333.
STRINGi9606.ENSP00000265517.

Chemistry

BindingDBiP55157.
ChEMBLiCHEMBL2364681.
DrugBankiDB01094. Hesperetin.
DB08827. Lomitapide.
SwissLipidsiSLP:000000411.

PTM databases

iPTMnetiP55157.
PhosphoSiteiP55157.

Polymorphism and mutation databases

BioMutaiMTTP.
DMDMi1709167.

Proteomic databases

MaxQBiP55157.
PaxDbiP55157.
PRIDEiP55157.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265517; ENSP00000265517; ENSG00000138823. [P55157-1]
ENST00000422897; ENSP00000407350; ENSG00000138823. [P55157-2]
ENST00000457717; ENSP00000400821; ENSG00000138823. [P55157-1]
GeneIDi4547.
KEGGihsa:4547.
UCSCiuc003hvb.4. human. [P55157-1]

Organism-specific databases

CTDi4547.
GeneCardsiMTTP.
HGNCiHGNC:7467. MTTP.
HPAiHPA054862.
MalaCardsiMTTP.
MIMi157147. gene.
200100. phenotype.
neXtProtiNX_P55157.
Orphaneti14. Abetalipoproteinemia.
426. Familial hypobetalipoproteinemia.
PharmGKBiPA164742099.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4337. Eukaryota.
ENOG410YKCW. LUCA.
GeneTreeiENSGT00390000011412.
HOGENOMiHOG000113688.
HOVERGENiHBG006416.
InParanoidiP55157.
KOiK14463.
PhylomeDBiP55157.
TreeFamiTF328754.

Enzyme and pathway databases

ReactomeiR-HSA-174800. Chylomicron-mediated lipid transport.

Miscellaneous databases

GeneWikiiMicrosomal_triglyceride_transfer_protein.
GenomeRNAii4547.
PROiP55157.
SOURCEiSearch...

Gene expression databases

BgeeiP55157.
CleanExiHS_MTTP.
ExpressionAtlasiP55157. baseline and differential.
GenevisibleiP55157. HS.

Family and domain databases

Gene3Di1.25.10.20. 1 hit.
2.30.230.10. 1 hit.
InterProiIPR015819. Lipid_transp_b-sht_shell.
IPR001747. Lipid_transpt_N.
IPR015816. Vitellinogen_b-sht_N.
IPR011030. Vitellinogen_superhlx.
[Graphical view]
PfamiPF01347. Vitellogenin_N. 1 hit.
[Graphical view]
SMARTiSM00638. LPD_N. 1 hit.
[Graphical view]
SUPFAMiSSF48431. SSF48431. 1 hit.
SSF56968. SSF56968. 1 hit.
PROSITEiPS51211. VITELLOGENIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Abetalipoproteinemia is caused by defects of the gene encoding the 97 kDa subunit of a microsomal triglyceride transfer protein."
    Shoulders C.C., Brett D.J., Bayliss J.D., Narcisi T.M.E., Jarmuz A., Grantham T.T., Leoni P.R.D., Bhattacharya S., Pease R.J., Cullen P.M., Levi S., Byfield P.G.H., Purkiss P., Scott J.
    Hum. Mol. Genet. 2:2109-2116(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Small intestine.
  2. "Cloning and gene defects in microsomal triglyceride transfer protein associated with abetalipoproteinaemia."
    Sharp D., Blinderman L., Combs K.A., Kienzle B., Ricci B., Wager-Smith K., Gil C.M., Turck C.W., Bouma M.-E., Rader D.J., Aggerbeck L.P., Gregg R.E., Gordon D.A., Wetterau J.R.
    Nature 365:65-69(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  3. "Human microsomal triglyceride transfer protein large subunit gene structure."
    Sharp D., Ricci B., Kienzle B., Lin M.C., Wetterau J.R.
    Biochemistry 33:9057-9061(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Tissue: Blood vessel.
  7. "Transcriptional regulation of human and hamster microsomal triglyceride transfer protein genes. Cell type-specific expression and response to metabolic regulators."
    Hagan D.L., Kienzle B., Jamil H., Hariharan N.
    J. Biol. Chem. 269:28737-28744(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, INDUCTION.
  8. "The abetalipoproteinemia gene is a member of the vitellogenin family and encodes an alpha-helical domain."
    Shoulders C.C., Narcisi T.M.E., Read J., Chester S.A., Brett D.J., Scott J., Anderson T.A., Levitt D.G., Banaszak L.J.
    Nat. Struct. Biol. 1:285-286(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: SIMILARITY TO VITELLOGENINS.
  9. "Mutations of the microsomal triglyceride-transfer-protein gene in abetalipoproteinemia."
    Narcisi T.M.E., Shoulders C.C., Chester S.A., Read J., Brett D.J., Harrison G.B., Grantham T.T., Fox M.F., Povey S., de Bruin T.W.A., Erkelens D.W., Muller D.P.R., Lloyd J.K., Scott J.
    Am. J. Hum. Genet. 57:1298-1310(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF CYS-878.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Loss of both phospholipid and triglyceride transfer activities of microsomal triglyceride transfer protein in abetalipoproteinemia."
    Khatun I., Walsh M.T., Hussain M.M.
    J. Lipid Res. 54:1541-1549(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH P4HB, SUBCELLULAR LOCATION, CHARACTERIZATION OF VARIANTS ABL HIS-540; ILE-590; GLU-746 AND TYR-780, CHARACTERIZATION OF VARIANT ALA-384.
  12. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  13. "A novel abetalipoproteinemia genotype. Identification of a missense mutation in the 97-kDa subunit of the microsomal triglyceride transfer protein that prevents complex formation with protein disulfide isomerase."
    Rehberg E.F., Samson-Bouma M.-E., Kienzle B., Blinderman L., Jamil H., Wetterau J.R., Aggerbeck L.P., Gordon D.A.
    J. Biol. Chem. 271:29945-29952(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL HIS-540, VARIANTS GLN-297 AND ALA-384, CHARACTERIZATION VARIANT ABL HIS-540, CHARACTERIZATION VARIANTS GLN-297 AND ALA-384, MUTAGENESIS OF ARG-540, FUNCTION, INVOLVEMENT IN ABL.
  14. "Microsomal triglyceride transfer protein (MTP) gene mutations in Canadian subjects with abetalipoproteinemia."
    Wang J., Hegele R.A.
    Hum. Mutat. 15:294-295(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS ABL HIS-540; ILE-590 AND GLU-746.
  15. "Novel mutations in the microsomal triglyceride transfer protein gene causing abetalipoproteinemia."
    Ohashi K., Ishibashi S., Osuga J., Tozawa R., Harada K., Yahagi N., Shionoiri F., Iizuka Y., Tamura Y., Nagai R., Illingworth D.R., Gotoda T., Yamada N.
    J. Lipid Res. 41:1199-1204(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL TYR-780.
  16. "Variants of the microsomal triglyceride transfer protein gene are associated with plasma cholesterol levels and body mass index."
    Ledmyr H., Karpe F., Lundahl B., McKinnon M., Skoglund-Andersson C., Ehrenborg E.
    J. Lipid Res. 43:51-58(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS HIS-95; THR-128; GLU-244 AND GLN-297.
  17. "Hypobetalipoproteinemia with an apparently recessive inheritance due to a 'de novo' mutation of apolipoprotein B."
    Lancellotti S., Di Leo E., Penacchioni J.Y., Balli F., Viola L., Bertolini S., Calandra S., Tarugi P.
    Biochim. Biophys. Acta 1688:61-67(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS THR-128; ILE-168 AND GLN-297.
  18. "Molecular and functional analysis of two new MTTP gene mutations in an atypical case of abetalipoproteinemia."
    Di Filippo M., Crehalet H., Samson-Bouma M.E., Bonnet V., Aggerbeck L.P., Rabes J.P., Gottrand F., Luc G., Bozon D., Sassolas A.
    J. Lipid Res. 53:548-555(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL HIS-435, CHARACTERIZATION OF VARIANT ABL HIS-435, FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF LEU-435.
  19. Cited for: VARIANTS ABL ARG-264; HIS-528; CYS-540 AND SER-649, CHARACTERIZATION OF VARIANTS ABL ARG-264; HIS-528; CYS-540; HIS-540 AND SER-649, FUNCTION, INTERACTION WITH APOB AND P4HB, MUTAGENESIS OF TYR-528.
  20. "A novel abetalipoproteinemia missense mutation highlights the importance of N-Terminal beta-barrel in microsomal triglyceride transfer protein function."
    Walsh M.T., Iqbal J., Josekutty J., Soh J., Di Leo E., Oezaydin E., Guenduez M., Tarugi P., Hussain M.M.
    Circ. Cardiovasc. Genet. 8:677-687(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT ABL VAL-169, CHARACTERIZATION OF VARIANT ABL VAL-169, FUNCTION, INTERACTION WITH APOB AND P4HB, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-169; LYS-187 AND LYS-189.

Entry informationi

Entry nameiMTP_HUMAN
AccessioniPrimary (citable) accession number: P55157
Secondary accession number(s): A8K428, Q08AM4, Q6P5T3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: June 8, 2016
This is version 147 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 4
    Human chromosome 4: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.